Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Pseudomonas aeruginosa |
Protein Variants | Comment | Organism |
---|---|---|
C1606A/S1607A | thioesterase domain active site double mutant, fails to turn over, but a monocyclic hydroxyphenyl-thiazolinyl-cysteine product continues to be released from subunit PchE | Pseudomonas aeruginosa |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.11 | - |
L-cysteine | pH 8.8, 30°C | Pseudomonas aeruginosa | |
0.537 | - |
L-cysteine | pH 8.8, 30°C | Pseudomonas aeruginosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(L-cysteinyl)adenylate + holo-[L-cysteinyl-carrier protein] | Pseudomonas aeruginosa | - |
AMP + L-cysteinyl-[L-cysteinyl-carrier protein] | - |
? | |
ATP + L-cysteine | Pseudomonas aeruginosa | - |
diphosphate + (L-cysteinyl)adenylate | - |
? | |
ATP + L-cysteine + holo-[L-cysteinyl-carrier protein] | Pseudomonas aeruginosa | - |
AMP + diphosphate + L-cysteinyl-[L-cysteinyl-carrier protein] | - |
? | |
additional information | Pseudomonas aeruginosa | the formation of cysteinyl-S-cysteinyl-carrier protein in PchE and PchF is an acylation in-cis, in which the cysteine transferase activity of each synthetase's adenylation domain loads cysteine on the cysteinyl-carrier protein domain located within the same polypeptide. No substrate: D-cysteine | ? | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | Q9RFM7 | isoform PchF | - |
Pseudomonas aeruginosa | Q9RFM8 | isoform PchE | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
phospholipoprotein | posttranslational modification by covalent attachment of the 4'-phosphopantetheine moiety of coenzyme A is essential for the biosynthetic competence. In PchE, possible domains for phosphopantetheinylation are an N-terminal aryl carrier protein domain and a C-terminal peptidyl carrier protein domain | Pseudomonas aeruginosa |
phospholipoprotein | posttranslational modification by covalent attachment of the 4'-phosphopantetheine moiety of coenzyme A is essential for the biosynthetic competence. PchF has a single carrier protein domain (PCP2), and is phosphopantetheinylated with a stoichiometry of 67% | Pseudomonas aeruginosa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(L-cysteinyl)adenylate + holo-[L-cysteinyl-carrier protein] | - |
Pseudomonas aeruginosa | AMP + L-cysteinyl-[L-cysteinyl-carrier protein] | - |
? | |
ATP + L-cysteine | - |
Pseudomonas aeruginosa | diphosphate + (L-cysteinyl)adenylate | - |
? | |
ATP + L-cysteine + holo-[L-cysteinyl-carrier protein] | - |
Pseudomonas aeruginosa | AMP + diphosphate + L-cysteinyl-[L-cysteinyl-carrier protein] | - |
? | |
additional information | the formation of cysteinyl-S-cysteinyl-carrier protein in PchE and PchF is an acylation in-cis, in which the cysteine transferase activity of each synthetase's adenylation domain loads cysteine on the cysteinyl-carrier protein domain located within the same polypeptide. No substrate: D-cysteine | Pseudomonas aeruginosa | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
non-ribosomal peptide synthetase | - |
Pseudomonas aeruginosa |
PChE | - |
Pseudomonas aeruginosa |
pchF | - |
Pseudomonas aeruginosa |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.63 | - |
L-cysteine | pH 8.8, 30°C | Pseudomonas aeruginosa | |
6.9 | - |
L-cysteine | pH 8.8, 30°C | Pseudomonas aeruginosa |
General Information | Comment | Organism |
---|---|---|
physiological function | protein PchD, PchE, and PchF are involved in biogenesis of the nonribosomal peptide siderophore pyochelin. PchE and PchF activate the cysteine as adenylate. PchD, PchE, and PchF produce the tricyclic acid hydroxyphenyl-thiazolyl-thiazolinyl-carboxylic acid. The three proteins contain three adenylation domains, one specific for salicylate activation and two specific for cysteine activation, and three carrier protein domains (two in PchE and one in PchF) that undergo posttranslational priming with phosphopantetheine to enable covalent tethering of salicyl and cysteinyl moieties as acyl-S-enzyme intermediates. Two cyclization domains (Cy1 in PchE and Cy2 in PchF) create the two amide linkages in the elongating chains and the cyclodehydrations of acylcysteine moieties into thiazolinyl rings. The ninth domain, the most downstream domain in PchF, is the chain-terminating, acyl-S-enzyme thioester hydrolase that releases the hydroxyphenyl-thiazolyl-thiazolinyl-carboxylic acid-S-enzyme intermediate to the tandem bis-heterocyclic acid product | Pseudomonas aeruginosa |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
6.7 | - |
L-cysteine | pH 8.8, 30°C | Pseudomonas aeruginosa | |
13.3 | - |
L-cysteine | pH 8.8, 30°C | Pseudomonas aeruginosa |